Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone deacetylase 8

Gene

HDAC8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility.5 Publications

Catalytic activityi

Hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone.

Cofactori

a divalent metal cationNote: Binds 1 divalent metal cation per subunit.

Enzyme regulationi

Its activity is inhibited by trichostatin A (TSA), suberoylanilide hydroxamic acid (SAHA), 3-(1-methyl-4-phenylacetyl-1H-2-pyrrolyl)-N-hydroxy-2-propenamide (APHA), 4-dimethylamino-N-(6-hydroxycarbamoyethyl)benzamide-N-hydroxy-7-(4-dimethylaminobenzoyl)aminoheptanamide (MS-344), 5-(4-methyl-benzoylamino)-biphenyl-3,4'-dicarboxylic acid 3-dimethylamide 4'-hydroxyamide (CRA-A) and butyrate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei101Substrate1
Active sitei143Proton acceptor1 Publication1
Binding sitei151Substrate; via carbonyl oxygen1
Metal bindingi178Divalent metal cation1 Publication1
Metal bindingi180Divalent metal cation1 Publication1
Metal bindingi267Divalent metal cation1 Publication1
Binding sitei306Substrate1

GO - Molecular functioni

  • chromatin binding Source: Ensembl
  • histone deacetylase activity Source: UniProtKB
  • Hsp70 protein binding Source: BHF-UCL
  • Hsp90 protein binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • cellular response to forskolin Source: Ensembl
  • cellular response to trichostatin A Source: Ensembl
  • chromatin assembly or disassembly Source: ProtInc
  • chromatin organization Source: UniProtKB
  • negative regulation of histone H3-K9 acetylation Source: Ensembl
  • negative regulation of osteoblast differentiation Source: Ensembl
  • negative regulation of protein ubiquitination Source: BHF-UCL
  • negative regulation of transcription by RNA polymerase II Source: ProtInc
  • regulation of cohesin loading Source: UniProtKB
  • regulation of protein stability Source: BHF-UCL
  • regulation of telomere maintenance Source: BHF-UCL
  • sister chromatid cohesion Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionChromatin regulator, Hydrolase, Repressor
Biological processTranscription, Transcription regulation
LigandMetal-binding

Enzyme and pathway databases

BRENDAi3.5.1.98 2681
ReactomeiR-HSA-2122947 NOTCH1 Intracellular Domain Regulates Transcription
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants
R-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants
R-HSA-3214815 HDACs deacetylate histones
SABIO-RKQ9BY41
SIGNORiQ9BY41

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 8 (EC:3.5.1.98)
Short name:
HD8
Gene namesi
Name:HDAC8
Synonyms:HDACL1
ORF Names:CDA07
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

EuPathDBiHostDB:ENSG00000147099.19
HGNCiHGNC:13315 HDAC8
MIMi300269 gene
neXtProtiNX_Q9BY41

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Cornelia de Lange syndrome 5 (CDLS5)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. It is characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation, hirsutism, gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies.
See also OMIM:300882
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069140180H → R in CDLS5. 1 PublicationCorresponds to variant dbSNP:rs397515416EnsemblClinVar.1
Natural variantiVAR_069141311T → M in CDLS5. 1 PublicationCorresponds to variant dbSNP:rs397515417EnsemblClinVar.1
Natural variantiVAR_069142320G → R in CDLS5. 1 PublicationCorresponds to variant dbSNP:rs398122909EnsemblClinVar.1
Natural variantiVAR_069143334H → R in CDLS5. 1 PublicationCorresponds to variant dbSNP:rs397515418EnsemblClinVar.1
Wilson-Turner X-linked mental retardation syndrome (WTS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA neurologic disorder characterized by severe intellectual disability, dysmorphic facial features, hypogonadism, short stature, and truncal obesity. Affected females have a milder phenotype than affected males.
See also OMIM:309585

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi39S → A: Enhances the deacetylase activity. 1 Publication1
Mutagenesisi39S → E: Decreases the deacetylase activity. 1 Publication1
Mutagenesisi101D → A: Complete loss of catalytical activity. Complete loss of catalytical activity; when associated with F-306. 2 Publications1
Mutagenesisi101D → E: Partial loss of catalytical activity. 2 Publications1
Mutagenesisi101D → L: Complete loss of catalytical activity. 2 Publications1
Mutagenesisi101D → N: Almost complete loss of catalytical activity. 2 Publications1
Mutagenesisi142 – 143HH → AA: Strongly reduces histone deacetylase activity. 1 Publication2
Mutagenesisi143H → A: Loss of catalytic activity. 1 Publication1
Mutagenesisi306Y → F: Loss of catalytic activity. Complete loss of catalytic activity; when associated with A-101. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation, Obesity

Organism-specific databases

DisGeNETi55869
GeneReviewsiHDAC8
MalaCardsiHDAC8
MIMi300882 phenotype
309585 phenotype
OpenTargetsiENSG00000147099
Orphaneti199 Cornelia de Lange syndrome
3459 Wilson-Turner syndrome
PharmGKBiPA37766

Chemistry databases

ChEMBLiCHEMBL3192
DrugBankiDB07350 (2E)-N-hydroxy-3-[1-methyl-4-(phenylacetyl)-1H-pyrrol-2-yl]prop-2-enamide
DB02565 4-Dimethylamino-N-(6-Hydroxycarbamoyethyl)Benzamide-N-Hydroxy-7-(4-Dimethyla Minobenzoyl)Aminoheptanamide
DB08168 7-AMINO-4-METHYL-CHROMEN-2-ONE
DB05015 Belinostat
DB02917 N-Hydroxy-4-(Methyl{[5-(2-Pyridinyl)-2-Thienyl]Sulfonyl}Amino)Benzamide
DB06603 Panobinostat
DB02546 Vorinostat
GuidetoPHARMACOLOGYi2619

Polymorphism and mutation databases

BioMutaiHDAC8
DMDMi29839394

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001147081 – 377Histone deacetylase 8Add BLAST377

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei39Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylated by PKA on serine 39. Phosphorylation reduces deacetylase activity observed preferentially on histones H3 and H4.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9BY41
MaxQBiQ9BY41
PaxDbiQ9BY41
PeptideAtlasiQ9BY41
PRIDEiQ9BY41

PTM databases

iPTMnetiQ9BY41
PhosphoSitePlusiQ9BY41

Expressioni

Tissue specificityi

Weakly expressed in most tissues. Expressed at higher level in heart, brain, kidney and pancreas and also in liver, lung, placenta, prostate and kidney.4 Publications

Gene expression databases

BgeeiENSG00000147099
CleanExiHS_HDAC8
ExpressionAtlasiQ9BY41 baseline and differential
GenevisibleiQ9BY41 HS

Organism-specific databases

HPAiHPA048560

Interactioni

Subunit structurei

Interacts with PEPB2-MYH11, a fusion protein consisting of the 165 N-terminal residues of CBF-beta (PEPB2) with the tail region of MYH11 produced by the inversion Inv(16)(p13q22), a translocation associated with acute myeloid leukemia of M4EO subtype. The PEPB2-MYH1 fusion protein also interacts with RUNX1, a well known transcriptional regulator, suggesting that the interaction with HDAC8 may participate in the conversion of RUNX1 into a constitutive transcriptional repressor. Interacts with CBFA2T3. Interacts with phosphorylated SMG5/EST1B; this interaction protects SMG5 from ubiquitin-mediated degradation. Associates with alpha-SMA (smooth muscle alpha-actin).4 Publications

GO - Molecular functioni

  • Hsp70 protein binding Source: BHF-UCL
  • Hsp90 protein binding Source: BHF-UCL
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120968, 36 interactors
ELMiQ9BY41
IntActiQ9BY41, 17 interactors
MINTiQ9BY41
STRINGi9606.ENSP00000362674

Chemistry databases

BindingDBiQ9BY41

Structurei

Secondary structure

1377
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi17 – 19Combined sources3
Helixi22 – 28Combined sources7
Turni29 – 31Combined sources3
Beta strandi32 – 34Combined sources3
Helixi37 – 47Combined sources11
Helixi50 – 53Combined sources4
Beta strandi54 – 57Combined sources4
Helixi64 – 67Combined sources4
Turni68 – 70Combined sources3
Helixi73 – 84Combined sources12
Beta strandi87 – 89Combined sources3
Turni91 – 97Combined sources7
Beta strandi99 – 102Combined sources4
Helixi108 – 127Combined sources20
Beta strandi128 – 130Combined sources3
Beta strandi132 – 136Combined sources5
Beta strandi153 – 155Combined sources3
Helixi157 – 165Combined sources9
Turni166 – 168Combined sources3
Beta strandi172 – 176Combined sources5
Beta strandi178 – 180Combined sources3
Helixi183 – 188Combined sources6
Turni189 – 191Combined sources3
Beta strandi193 – 202Combined sources10
Beta strandi207 – 209Combined sources3
Helixi220 – 222Combined sources3
Beta strandi225 – 231Combined sources7
Helixi237 – 255Combined sources19
Beta strandi258 – 263Combined sources6
Helixi266 – 268Combined sources3
Helixi281 – 292Combined sources12
Beta strandi297 – 301Combined sources5
Helixi308 – 323Combined sources16
Helixi337 – 340Combined sources4
Turni341 – 343Combined sources3
Helixi359 – 372Combined sources14
Turni374 – 376Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T64X-ray1.90A/B1-377[»]
1T67X-ray2.31A1-377[»]
1T69X-ray2.91A1-377[»]
1VKGX-ray2.20A/B1-377[»]
1W22X-ray2.50A/B1-377[»]
2V5WX-ray2.00A/B1-377[»]
2V5XX-ray2.25A/B1-377[»]
3EW8X-ray1.80A1-377[»]
3EWFX-ray2.50A/B/C/D1-377[»]
3EZPX-ray2.65A/B1-377[»]
3EZTX-ray2.85A/B1-377[»]
3F06X-ray2.55A/B1-377[»]
3F07X-ray3.30A/B/C1-377[»]
3F0RX-ray2.54A/B/C1-377[»]
3MZ3X-ray3.20A/B1-377[»]
3MZ4X-ray1.84A/B1-377[»]
3MZ6X-ray2.00A1-377[»]
3MZ7X-ray1.90A1-377[»]
3RQDX-ray2.14A/B1-377[»]
3SFFX-ray2.00A1-377[»]
3SFHX-ray2.70A1-377[»]
4QA0X-ray2.24A/B1-377[»]
4QA1X-ray1.92A/B/C/D1-377[»]
4QA2X-ray2.38A/B1-377[»]
4QA3X-ray2.88A/B1-377[»]
4QA4X-ray1.98A1-377[»]
4QA5X-ray1.76A/B1-377[»]
4QA6X-ray2.05A/B1-377[»]
4QA7X-ray2.31A1-377[»]
4RN0X-ray1.76A/B1-377[»]
4RN1X-ray2.18A/B1-377[»]
4RN2X-ray2.39A/B1-377[»]
5BWZX-ray1.59A/B1-377[»]
5D1BX-ray2.90A/B1-377[»]
5D1CX-ray1.42A/B1-377[»]
5D1DX-ray2.01A/B1-377[»]
5DC5X-ray1.94A/B1-377[»]
5DC6X-ray1.55A/B1-377[»]
5DC7X-ray2.30A/B1-377[»]
5DC8X-ray1.30A/B1-377[»]
5FCWX-ray1.98A/B1-377[»]
5THSX-ray1.90A/B1-377[»]
5THTX-ray2.41A/B/C/D1-377[»]
5THUX-ray1.95A/B1-377[»]
5THVX-ray1.87A/B1-377[»]
5VI6X-ray1.24A8-377[»]
ProteinModelPortaliQ9BY41
SMRiQ9BY41
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BY41

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni14 – 324Histone deacetylaseAdd BLAST311

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1342 Eukaryota
COG0123 LUCA
GeneTreeiENSGT00910000144047
HOGENOMiHOG000225180
HOVERGENiHBG057112
InParanoidiQ9BY41
KOiK11405
OMAiCGYDANA
OrthoDBiEOG091G0A9R
PhylomeDBiQ9BY41
TreeFamiTF106175

Family and domain databases

Gene3Di3.40.800.20, 1 hit
InterProiView protein in InterPro
IPR000286 His_deacetylse
IPR003084 His_deacetylse_1
IPR023801 His_deacetylse_dom
IPR037138 His_deacetylse_dom_sf
IPR023696 Ureohydrolase_dom_sf
PANTHERiPTHR10625 PTHR10625, 1 hit
PfamiView protein in Pfam
PF00850 Hist_deacetyl, 1 hit
PIRSFiPIRSF037913 His_deacetylse_1, 1 hit
PRINTSiPR01270 HDASUPER
PR01271 HISDACETLASE
SUPFAMiSSF52768 SSF52768, 1 hit

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BY41-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEEPEEPADS GQSLVPVYIY SPEYVSMCDS LAKIPKRASM VHSLIEAYAL
60 70 80 90 100
HKQMRIVKPK VASMEEMATF HTDAYLQHLQ KVSQEGDDDH PDSIEYGLGY
110 120 130 140 150
DCPATEGIFD YAAAIGGATI TAAQCLIDGM CKVAINWSGG WHHAKKDEAS
160 170 180 190 200
GFCYLNDAVL GILRLRRKFE RILYVDLDLH HGDGVEDAFS FTSKVMTVSL
210 220 230 240 250
HKFSPGFFPG TGDVSDVGLG KGRYYSVNVP IQDGIQDEKY YQICESVLKE
260 270 280 290 300
VYQAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY ILQWQLATLI
310 320 330 340 350
LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP
360 370
SCRPDRNEPH RIQQILNYIK GNLKHVV
Length:377
Mass (Da):41,758
Last modified:April 11, 2003 - v2
Checksum:iCAA1B91894FB5013
GO
Isoform 4 (identifier: Q9BY41-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     56-146: Missing.

Note: No experimental confirmation available.
Show »
Length:286
Mass (Da):31,935
Checksum:iB69361BAC77E90E2
GO
Isoform 5 (identifier: Q9BY41-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     246-272: SVLKEVYQAFNPKAVVLQLGADTIAGD → RYEPPAPNPGL
     273-377: Missing.

Note: No experimental confirmation available.
Show »
Length:256
Mass (Da):28,353
Checksum:i175AB23C2589926F
GO
Isoform 6 (identifier: Q9BY41-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     56-146: Missing.
     185-210: Missing.
     246-256: SVLKEVYQAFN → RYEPPAPNPGL
     257-377: Missing.

Note: Gene prediction based on EST data.
Show »
Length:139
Mass (Da):15,685
Checksum:iE46FD4F32AAABC43
GO
Isoform 7 (identifier: Q9BY41-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     147-158: DEASGFCYLNDA → ETCVYVALYKAF
     159-377: Missing.

Note: Gene prediction based on EST data.
Show »
Length:158
Mass (Da):17,439
Checksum:iF7EFADF18566BB00
GO
Isoform 8 (identifier: Q9BY41-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     147-377: Missing.

Note: No experimental confirmation available.
Show »
Length:146
Mass (Da):16,050
Checksum:i5234C861058EAE1B
GO

Sequence cautioni

The sequence AAK14930 differs from that shown. Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti31L → P in AAH50433 (PubMed:15489334).Curated1
Sequence conflicti179L → V no nucleotide entry (PubMed:10756090).Curated1
Sequence conflicti223R → W in AAF73428 (PubMed:10926844).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069140180H → R in CDLS5. 1 PublicationCorresponds to variant dbSNP:rs397515416EnsemblClinVar.1
Natural variantiVAR_069141311T → M in CDLS5. 1 PublicationCorresponds to variant dbSNP:rs397515417EnsemblClinVar.1
Natural variantiVAR_069142320G → R in CDLS5. 1 PublicationCorresponds to variant dbSNP:rs398122909EnsemblClinVar.1
Natural variantiVAR_069143334H → R in CDLS5. 1 PublicationCorresponds to variant dbSNP:rs397515418EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04342656 – 146Missing in isoform 4 and isoform 6. 1 PublicationAdd BLAST91
Alternative sequenceiVSP_047502147 – 377Missing in isoform 8. 1 PublicationAdd BLAST231
Alternative sequenceiVSP_046832147 – 158DEASG…YLNDA → ETCVYVALYKAF in isoform 7. CuratedAdd BLAST12
Alternative sequenceiVSP_046833159 – 377Missing in isoform 7. CuratedAdd BLAST219
Alternative sequenceiVSP_046834185 – 210Missing in isoform 6. CuratedAdd BLAST26
Alternative sequenceiVSP_043427246 – 272SVLKE…TIAGD → RYEPPAPNPGL in isoform 5. 1 PublicationAdd BLAST27
Alternative sequenceiVSP_046835246 – 256SVLKEVYQAFN → RYEPPAPNPGL in isoform 6. CuratedAdd BLAST11
Alternative sequenceiVSP_046836257 – 377Missing in isoform 6. CuratedAdd BLAST121
Alternative sequenceiVSP_007177273 – 377Missing in isoform 5. 1 PublicationAdd BLAST105

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF230097 mRNA Translation: AAF73076.1
AF245664 mRNA Translation: AAF73428.1
AJ277724 mRNA Translation: CAB90213.1
BQ189619 mRNA No translation available.
AK296641 mRNA Translation: BAG59242.1
AK300895 mRNA Translation: BAG62534.1
AA376331 mRNA No translation available.
AI159768 mRNA No translation available.
T99283 mRNA No translation available.
AF212246 mRNA Translation: AAK14930.1 Sequence problems.
AL133500 Genomic DNA No translation available.
BX295542 Genomic DNA No translation available.
BC050433 mRNA Translation: AAH50433.1
CCDSiCCDS14420.1 [Q9BY41-1]
CCDS55448.1 [Q9BY41-6]
CCDS55449.1 [Q9BY41-4]
CCDS55450.1 [Q9BY41-8]
CCDS55451.1 [Q9BY41-5]
CCDS55452.1 [Q9BY41-7]
RefSeqiNP_001159890.1, NM_001166418.1 [Q9BY41-4]
NP_001159891.1, NM_001166419.1 [Q9BY41-5]
NP_001159892.1, NM_001166420.1 [Q9BY41-8]
NP_001159894.1, NM_001166422.1 [Q9BY41-7]
NP_001159920.1, NM_001166448.1 [Q9BY41-6]
NP_060956.1, NM_018486.2 [Q9BY41-1]
UniGeneiHs.310536

Genome annotation databases

EnsembliENST00000373554; ENSP00000362655; ENSG00000147099 [Q9BY41-8]
ENST00000373556; ENSP00000362657; ENSG00000147099 [Q9BY41-7]
ENST00000373559; ENSP00000362660; ENSG00000147099 [Q9BY41-6]
ENST00000373573; ENSP00000362674; ENSG00000147099 [Q9BY41-1]
ENST00000373589; ENSP00000362691; ENSG00000147099 [Q9BY41-4]
ENST00000439122; ENSP00000414486; ENSG00000147099 [Q9BY41-5]
GeneIDi55869
KEGGihsa:55869
UCSCiuc004eau.3 human [Q9BY41-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiHDAC8_HUMAN
AccessioniPrimary (citable) accession number: Q9BY41
Secondary accession number(s): A6ND12
, A6ND61, A6NET3, A6NJR3, A8MQ62, B4DKN0, B4DV22, Q86VC8, Q9NP76, Q9NYH4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: April 11, 2003
Last modified: March 28, 2018
This is version 160 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health